Functionalizing Nisin with a Sugar Moiety Improves Its Solubility and Results in an Altered Antibacterial Spectrum and Mode of Action.

ABSTRACT: Glycosylation, a widespread post-translational modification, is present in all kingdoms of life. Despite the extensive structural diversity found in ribosomally synthesized and post-translationally modified peptides (RiPPs), only a few glycosylated bacteriocins, known as glycocins, have been identified. Notably, glycocins such as glycocin F, ASM1, and enterocin F4-9, exhibit antimicrobial properties and distinct glycoactivity, indicating that glycosylation is crucial for their bioactivity. The development of practical, and widely applicable systems for glycosylation of RiPPs is therefore highly desirable. In this study, we introduce an expression system that utilizes Lactococcus lactis as a host for the efficient incorporation of the noncanonical amino acid homopropargylglycine (Hpg

SUBMITTER: Guo L 

PROVIDER: S-EPMC12455637 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature